title: Interaction of bovine estrogen receptor with immobilized zinc.
abstract: The metal-binding properties of partially purified untransformed or salt-dissociated bovine estrogen receptors were studied using zinc-chelated iminodiacetic acid gels. Only the salt-dissociated 5S receptor is retained by the metal-chelated resin, and this interaction is dependent on the presence of dithiothreitol. The untransformed 9S receptor is not retained, indicating that the zinc-interacting amino acid residues may be masked by receptor-associated proteins such as 90K heat-shock protein or because of an unfavorable receptor conformation.
authors.affiliation: Department of Obstetrics and Gynaecology, University of Western Australia, King Edward Memorial Hospital for Women, Subiaco.
authors.forename: H C
authors.initials: HC
authors.lastname: Atkinson
authors.forename: T
authors.initials: T
authors.lastname: Ratajczak
authors.forename: R
authors.initials: R
authors.lastname: Hähnel
mesh_terms: D000818:Animals; D002417:Cattle; D002614:Chelating Agents; D002846:Chromatography, Affinity; D003600:Cytosol / Q000737:chemistry; D004229:Dithiothreitol; D005782:Gels; D006493:Heparin; D007098:Imino Acids; D011960:Receptors, Estrogen / Q000737:chemistry*; D012588:Scintillation Counting; D012685:Sepharose; D014461:Ultracentrifugation; D015032:Zinc / Q000737:chemistry*
chemical_list: D002614:Chelating Agents; D005782:Gels; D007098:Imino Acids; D011960:Receptors, Estrogen; D006493:Heparin; D012685:Sepharose; D015032:Zinc; D004229:Dithiothreitol; C008109:iminodiacetic acid